NDLI: Crystallization and preliminary crystallographic analysis of cysteine synthase from Entamoeba histolytica.

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Crystallization and preliminary crystallographic analysis of cysteine synthase from Entamoeba histolytica.

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Crystallization and preliminary crystallographic analysis of cysteine synthase from Entamoeba histolytica.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Krishna, Chinthalapudi Jain, Ruchi Kashav, Tara Wadhwa, Dinakar Alam, Neelima Gourinath, S.
Description	Country affiliation: India Author Affiliation: Krishna C ( School of Life Sciences, Jawaharlal Nehru University, New Delhi, India.)
Abstract	Entamoeba histolytica, the causative agent of human amoebiasis, is essentially anaerobic, requiring a small amount of oxygen for growth. It cannot tolerate the higher concentration of oxygen present in human tissues or blood. However, during tissue invasion it is exposed to a higher level of oxygen, leading to oxygen stress. Cysteine, which is a vital thiol in E. histolytica, plays an essential role in its oxygen-defence mechanisms. The major route of cysteine biosynthesis in this parasite is the condensation of O-acetylserine with sulfide by the de novo cysteine-biosynthetic pathway, which involves cysteine synthase (EhCS) as a key enzyme. In this study, EhCS was cloned, expressed in Escherichia coli and purified by affinity and size-exclusion chromatography. The purified protein was crystallized in space group P4(1) with two molecules per asymmetric unit and a complete data set was collected to a resolution of 1.86 A. A molecular-replacement solution was obtained using the Salmonella typhimurium O-acetylserine sulfhydrylase structure as a probe and had a correlation coefficient of 37.7% and an R factor of 48.8%.
File Format	HTM / HTML
ISSN	2053230X
e-ISSN	17443091
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Issue Number	Pt 6
Volume Number	63
Language	English
Publisher	Wiley
Publisher Date	2007-06-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Cysteine Synthase Chemistry Entamoeba Histolytica Enzymology Animals Crystallization Crystallography, X-ray Isolation & Purification Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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